data_6252 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N Resonance Assignments of the EscJ Protein, a Structural Component of the Type III Secretion System of Enteropathogenic E. coli (EPEC) ; _BMRB_accession_number 6252 _BMRB_flat_file_name bmr6252.str _Entry_type original _Submission_date 2004-06-25 _Accession_date 2004-06-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Prasannan Sunil . . 2 Simpson Peter J. . 3 Wilson Rebecca K. . 4 Frankel Gad . . 5 Matthews Stephen J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 291 "13C chemical shifts" 446 "15N chemical shifts" 145 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-12-15 update BMRB 'updated citation' 2004-08-03 original author 'Original Release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C, 15N Resonance Assignments of the EscJ Protein, a Structural Component of the Type III Secretion System of Enteropathogenic E. coli (EPEC) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Prasannan Sunil . . 2 Simpson Peter J. . 3 Wilson Rebecca K. . 4 Crepin Valerie F. . 5 Frankel Gad . . 6 Matthews Stephen J. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 30 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 387 _Page_last 388 _Year 2004 _Details . loop_ _Keyword EscJ NMR 'Type III Secretion' 'Triple Resonance' stop_ save_ ################################## # Molecular system description # ################################## save_system_EscJ _Saveframe_category molecular_system _Mol_system_name 'EscJ protein' _Abbreviation_common EscJ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'EscJ monomer' $EscJ stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Periplasmic component of Type III Secretion System of Enteropathogenic E. coli' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EscJ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Type III Secretion System component EscJ' _Abbreviation_common EscJ _Molecular_mass 18544 _Mol_thiol_state 'not present' _Details ; Sequence and M.W. minus linker and His Tag with sequence MHHHHHHSSGLVMPRGSHM ; ############################## # Polymer residue sequence # ############################## _Residue_count 170 _Mol_residue_sequence ; KEQLYTGLTEKEANQMQALL LSNDVNVSKEMDKSGNMTLS VEKEDFVRAITILNNNGFPK KKFADIEVIFPPSQLVASPS QENAKINYLKEQDIERLLSK IPGVIDCSVSLNVNNNESQP SSAAVLVISSPEVNLAPSVI QIKNLVKNSVDDLKLENISV VIKSSSGQDG ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 GLU 3 GLN 4 LEU 5 TYR 6 THR 7 GLY 8 LEU 9 THR 10 GLU 11 LYS 12 GLU 13 ALA 14 ASN 15 GLN 16 MET 17 GLN 18 ALA 19 LEU 20 LEU 21 LEU 22 SER 23 ASN 24 ASP 25 VAL 26 ASN 27 VAL 28 SER 29 LYS 30 GLU 31 MET 32 ASP 33 LYS 34 SER 35 GLY 36 ASN 37 MET 38 THR 39 LEU 40 SER 41 VAL 42 GLU 43 LYS 44 GLU 45 ASP 46 PHE 47 VAL 48 ARG 49 ALA 50 ILE 51 THR 52 ILE 53 LEU 54 ASN 55 ASN 56 ASN 57 GLY 58 PHE 59 PRO 60 LYS 61 LYS 62 LYS 63 PHE 64 ALA 65 ASP 66 ILE 67 GLU 68 VAL 69 ILE 70 PHE 71 PRO 72 PRO 73 SER 74 GLN 75 LEU 76 VAL 77 ALA 78 SER 79 PRO 80 SER 81 GLN 82 GLU 83 ASN 84 ALA 85 LYS 86 ILE 87 ASN 88 TYR 89 LEU 90 LYS 91 GLU 92 GLN 93 ASP 94 ILE 95 GLU 96 ARG 97 LEU 98 LEU 99 SER 100 LYS 101 ILE 102 PRO 103 GLY 104 VAL 105 ILE 106 ASP 107 CYS 108 SER 109 VAL 110 SER 111 LEU 112 ASN 113 VAL 114 ASN 115 ASN 116 ASN 117 GLU 118 SER 119 GLN 120 PRO 121 SER 122 SER 123 ALA 124 ALA 125 VAL 126 LEU 127 VAL 128 ILE 129 SER 130 SER 131 PRO 132 GLU 133 VAL 134 ASN 135 LEU 136 ALA 137 PRO 138 SER 139 VAL 140 ILE 141 GLN 142 ILE 143 LYS 144 ASN 145 LEU 146 VAL 147 LYS 148 ASN 149 SER 150 VAL 151 ASP 152 ASP 153 LEU 154 LYS 155 LEU 156 GLU 157 ASN 158 ILE 159 SER 160 VAL 161 VAL 162 ILE 163 LYS 164 SER 165 SER 166 SER 167 GLY 168 GLN 169 ASP 170 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1YJ7 "Crystal Structure Of Enteropathogenic E.Coli (Epec) Type Iii Secretion System Protein Escj" 100.00 171 98.24 98.24 2.20e-111 DBJ BAB37996 "type III secretion system EscJ protein [Escherichia coli O157:H7 str. Sakai]" 100.00 190 100.00 100.00 7.71e-114 DBJ BAG66748 "T3SS structure protein EscJ [Escherichia coli O111:H-]" 100.00 190 98.82 100.00 2.20e-112 DBJ BAI28408 "T3SS structure protein EscJ [Escherichia coli O26:H11 str. 11368]" 100.00 190 98.82 100.00 2.20e-112 DBJ BAI32346 "T3SS structure protein EscJ [Escherichia coli O103:H2 str. 12009]" 100.00 190 98.82 100.00 2.20e-112 DBJ BAI37542 "T3SS structure protein EscJ [Escherichia coli O111:H- str. 11128]" 100.00 190 100.00 100.00 7.71e-114 EMBL CAC81857 "EscJ protein [Escherichia coli]" 100.00 190 98.82 100.00 2.20e-112 EMBL CAG17525 "EscJ protein [Escherichia coli]" 100.00 190 99.41 100.00 5.10e-113 EMBL CAI43879 "EscJ protein [Escherichia coli]" 100.00 190 98.82 100.00 2.20e-112 EMBL CAR47976 "EscJ protein [Escherichia coli]" 100.00 190 98.82 100.00 2.20e-112 EMBL CAR48046 "EscJ protein [Escherichia coli]" 100.00 190 98.82 100.00 2.20e-112 GB AAC31518 "L0039 [Escherichia coli O157:H7 str. EDL933]" 100.00 190 100.00 100.00 7.71e-114 GB AAC38379 "EscJ [Escherichia coli]" 100.00 190 100.00 100.00 7.71e-114 GB AAG58837 "escJ [Escherichia coli O157:H7 str. EDL933]" 100.00 190 100.00 100.00 7.71e-114 GB AAK26710 "EscJ [Escherichia coli]" 100.00 190 98.82 100.00 2.20e-112 GB AAL30751 "putative EscJ protein [Escherichia coli]" 100.00 190 98.24 100.00 1.11e-111 REF NP_290273 "hypothetical protein Z5124 [Escherichia coli O157:H7 str. EDL933]" 100.00 190 100.00 100.00 7.71e-114 REF NP_312600 "EscJ [Escherichia coli O157:H7 str. Sakai]" 100.00 190 100.00 100.00 7.71e-114 REF WP_000408508 "hypothetical protein, partial [Escherichia coli]" 59.41 101 100.00 100.00 4.95e-60 REF WP_000716186 "EscJ [Escherichia coli]" 100.00 190 99.41 100.00 5.10e-113 REF WP_000716187 "EscJ [Escherichia coli]" 100.00 190 99.41 99.41 2.56e-113 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Fraction _Gene_mnemonic $EscJ 'E. coli' 562 Eubacteria . Escherichia coli O127:H6 periplasm escJ stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $EscJ 'recombinant technology' . . . . . 'grown in BL21 DE3, plasmid pET28a - His-Tag' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Isotopic_labeling $EscJ . mM 0.25 '[U-13C; U-15N]' 'sodium chloride' 30 mM . . Imidazole 50 mM . . 'sodium phosphate' 50 mM . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Isotopic_labeling $EscJ . mM 0.25 '[U-13C; U-15N]' 'sodium chloride' 30 mM . . Imidazole 30 mM . . 'sodium phosphate' 50 mM . . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Isotopic_labeling $EscJ . mM 0.25 '[U-15N]; [13C]-Val, Ile, (non-backbone) Leu' 'sodium chloride' 30 mM . . Imidazole 50 mM . . 'sodium phosphate' 50 mM . . stop_ save_ ############################ # Computer software used # ############################ save_XWIN-NMR _Saveframe_category software _Name XWIN-NMR _Version . loop_ _Task 'Spectral Processing' stop_ _Details . save_ save_AURELIA _Saveframe_category software _Name AURELIA _Version . loop_ _Task Peak-picking 'Sequential Assigment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCB _Sample_label . save_ save_HN(CO)CACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCO_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HBHA(CBCACO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NH _Sample_label . save_ save_HCCH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCB _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NH _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details 'z-shielded gradient triple resonance cryoprobe' save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 na temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP H 1 'methyl protons' ppm 0 internal direct cylindrical internal parallel 1.000000000 TSP N 15 'methyl protons' ppm 0 internal indirect cylindrical internal parallel 0.101329118 TSP C 13 'methyl protons' ppm 0 internal indirect cylindrical internal parallel 0.25144953 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HSQC HNCA HN(CO)CA HNCACB CBCA(CO)NH HNCB HN(CO)CACB HN(CA)CO HNCO HBHA(CBCACO)NH HCCH-TOCSY stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'EscJ monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 LYS H H 8.19 0.01 1 2 . 1 LYS N N 121.41 0.24 1 3 . 1 LYS HA H 4.33 0.01 1 4 . 1 LYS CA C 55.62 0.01 1 5 . 1 LYS CB C 34.37 0.01 1 6 . 1 LYS C C 175.66 0.01 1 7 . 2 GLU H H 8.94 0.01 1 8 . 2 GLU N N 120.93 0.24 1 9 . 2 GLU HA H 4.34 0.01 1 10 . 2 GLU CA C 54.32 0.01 1 11 . 2 GLU CB C 31.79 0.01 1 12 . 2 GLU C C 175.72 0.01 1 13 . 3 GLN H H 8.62 0.01 5 14 . 3 GLN N N 123.54 0.24 5 15 . 3 GLN HA H 4.09 0.01 1 16 . 3 GLN CA C 56.81 0.01 1 17 . 3 GLN CB C 29.62 0.01 1 18 . 3 GLN C C 175.35 0.01 1 19 . 4 LEU H H 9.17 0.01 1 20 . 4 LEU N N 125.68 0.24 1 21 . 4 LEU HA H 4.19 0.01 1 22 . 4 LEU CA C 55.57 0.01 1 23 . 4 LEU CB C 43.58 0.01 1 24 . 4 LEU C C 174.38 0.01 1 25 . 5 TYR H H 6.90 0.01 1 26 . 5 TYR N N 110.03 0.24 1 27 . 5 TYR HA H 4.79 0.01 1 28 . 5 TYR CA C 57.22 0.01 1 29 . 5 TYR CB C 45.13 0.01 1 30 . 5 TYR C C 173.83 0.01 1 31 . 6 THR H H 8.59 0.01 1 32 . 6 THR N N 112.87 0.24 1 33 . 6 THR HA H 5.02 0.01 1 34 . 6 THR CA C 59.39 0.01 1 35 . 6 THR CB C 70.66 0.01 1 36 . 6 THR C C 174.15 0.01 1 37 . 7 GLY H H 8.72 0.01 1 38 . 7 GLY N N 109.08 0.24 1 39 . 7 GLY HA2 H 3.54 0.01 1 40 . 7 GLY HA3 H 3.88 0.01 1 41 . 7 GLY CA C 46.16 0.01 1 42 . 7 GLY C C 175.06 0.01 1 43 . 8 LEU H H 8.42 0.01 5 44 . 8 LEU N N 118.80 0.24 5 45 . 8 LEU HA H 4.46 0.01 1 46 . 8 LEU CA C 53.67 0.01 1 47 . 8 LEU CB C 43.86 0.01 1 48 . 8 LEU C C 178.30 0.01 1 49 . 9 THR H H 8.89 0.01 1 50 . 9 THR N N 111.92 0.24 1 51 . 9 THR HA H 4.54 0.01 1 52 . 9 THR CA C 60.62 0.01 1 53 . 9 THR CB C 70.59 0.01 1 54 . 9 THR C C 175.60 0.01 1 55 . 10 GLU H H 8.77 0.01 1 56 . 10 GLU N N 121.88 0.24 1 57 . 10 GLU HA H 3.83 0.01 1 58 . 10 GLU CA C 60.05 0.01 1 59 . 10 GLU CB C 29.30 0.01 1 60 . 10 GLU C C 178.23 0.01 1 61 . 11 LYS H H 8.20 0.01 1 62 . 11 LYS N N 117.37 0.24 1 63 . 11 LYS HA H 3.92 0.01 1 64 . 11 LYS CA C 59.39 0.01 1 65 . 11 LYS CB C 32.41 0.01 1 66 . 11 LYS C C 179.24 0.01 1 67 . 12 GLU H H 7.64 0.01 5 68 . 12 GLU N N 119.51 0.24 5 69 . 12 GLU HA H 4.07 0.01 1 70 . 12 GLU CA C 59.31 0.01 1 71 . 12 GLU CB C 29.63 0.01 1 72 . 12 GLU C C 179.05 0.01 1 73 . 13 ALA H H 8.77 0.01 1 74 . 13 ALA N N 120.46 0.24 1 75 . 13 ALA HA H 3.78 0.01 1 76 . 13 ALA CA C 55.01 0.01 1 77 . 13 ALA CB C 17.94 0.01 1 78 . 13 ALA C C 179.39 0.01 1 79 . 14 ASN H H 8.41 0.01 1 80 . 14 ASN N N 116.19 0.24 1 81 . 14 ASN HA H 4.40 0.01 1 82 . 14 ASN CA C 55.62 0.01 1 83 . 14 ASN CB C 37.12 0.01 1 84 . 14 ASN C C 178.84 0.01 1 85 . 15 GLN H H 7.73 0.01 1 86 . 15 GLN N N 120.70 0.24 1 87 . 15 GLN HA H 4.09 0.01 1 88 . 15 GLN CA C 58.76 0.01 1 89 . 15 GLN CB C 28.79 0.01 1 90 . 15 GLN C C 179.37 0.01 1 91 . 16 MET H H 8.12 0.01 5 92 . 16 MET N N 118.80 0.24 5 93 . 16 MET HA H 3.46 0.01 1 94 . 16 MET CA C 59.29 0.01 1 95 . 16 MET CB C 33.68 0.01 1 96 . 16 MET C C 177.18 0.01 1 97 . 17 GLN H H 8.75 0.01 1 98 . 17 GLN N N 109.08 0.24 1 99 . 17 GLN HA H 3.63 0.01 1 100 . 17 GLN CA C 59.29 0.01 1 101 . 17 GLN CB C 28.49 0.01 1 102 . 17 GLN C C 177.02 0.01 1 103 . 18 ALA H H 7.95 0.01 1 104 . 18 ALA N N 118.80 0.24 1 105 . 18 ALA HA H 3.94 0.01 1 106 . 18 ALA CA C 55.06 0.01 1 107 . 18 ALA CB C 17.45 0.01 1 108 . 18 ALA C C 180.49 0.01 1 109 . 19 LEU H H 7.42 0.01 1 110 . 19 LEU N N 119.27 0.24 1 111 . 19 LEU HA H 4.02 0.01 1 112 . 19 LEU CA C 57.27 0.01 1 113 . 19 LEU CB C 41.49 0.01 1 114 . 19 LEU C C 179.76 0.01 1 115 . 20 LEU H H 8.06 0.01 1 116 . 20 LEU N N 120.70 0.24 1 117 . 20 LEU HA H 3.80 0.01 1 118 . 20 LEU CA C 58.47 0.01 1 119 . 20 LEU CB C 40.13 0.01 1 120 . 20 LEU C C 179.55 0.01 1 121 . 21 LEU H H 8.83 0.01 5 122 . 21 LEU N N 121.65 0.24 5 123 . 21 LEU HA H 4.09 0.01 1 124 . 21 LEU CA C 58.14 0.01 1 125 . 21 LEU CB C 41.49 0.01 1 126 . 21 LEU C C 182.00 0.01 1 127 . 22 SER H H 7.95 0.01 1 128 . 22 SER N N 114.53 0.24 1 129 . 22 SER HA H 4.27 0.01 1 130 . 22 SER CA C 61.19 0.01 1 131 . 22 SER CB C 62.72 0.01 1 132 . 22 SER C C 174.12 0.01 1 133 . 23 ASN H H 7.49 0.01 1 134 . 23 ASN N N 119.51 0.24 1 135 . 23 ASN HA H 4.69 0.01 1 136 . 23 ASN CA C 53.51 0.01 1 137 . 23 ASN CB C 41.16 0.01 1 138 . 23 ASN C C 172.50 0.01 1 139 . 24 ASP H H 7.91 0.01 1 140 . 24 ASP N N 114.06 0.24 1 141 . 24 ASP HA H 4.19 0.01 1 142 . 24 ASP CA C 55.47 0.01 1 143 . 24 ASP CB C 38.87 0.01 1 144 . 24 ASP C C 174.33 0.01 1 145 . 25 VAL H H 7.76 0.01 5 146 . 25 VAL N N 119.04 0.24 5 147 . 25 VAL HA H 3.98 0.01 1 148 . 25 VAL CA C 60.95 0.01 1 149 . 25 VAL CB C 32.33 0.01 1 150 . 25 VAL C C 174.54 0.01 1 151 . 26 ASN H H 8.72 0.01 1 152 . 26 ASN N N 124.73 0.24 1 153 . 26 ASN HA H 4.50 0.01 1 154 . 26 ASN CA C 53.10 0.01 1 155 . 26 ASN CB C 38.05 0.01 1 156 . 26 ASN C C 174.54 0.01 1 157 . 27 VAL H H 7.50 0.01 1 158 . 27 VAL N N 120.93 0.24 1 159 . 27 VAL HA H 4.83 0.01 1 160 . 27 VAL CA C 58.49 0.01 1 161 . 27 VAL CB C 34.45 0.01 1 162 . 27 VAL C C 173.71 0.01 1 163 . 28 SER H H 8.83 0.01 5 164 . 28 SER N N 121.65 0.24 5 165 . 28 SER HA H 4.69 0.01 1 166 . 28 SER CA C 56.69 0.01 1 167 . 28 SER CB C 64.46 0.01 1 168 . 28 SER C C 172.31 0.01 1 169 . 29 LYS H H 8.71 0.01 1 170 . 29 LYS N N 125.44 0.24 1 171 . 29 LYS HA H 5.25 0.01 1 172 . 29 LYS CA C 54.32 0.01 1 173 . 29 LYS CB C 35.44 0.01 1 174 . 29 LYS C C 174.72 0.01 1 175 . 30 GLU H H 8.48 0.01 1 176 . 30 GLU N N 123.78 0.24 1 177 . 30 GLU HA H 4.56 0.01 1 178 . 30 GLU CA C 54.41 0.01 1 179 . 30 GLU CB C 33.88 0.01 1 180 . 30 GLU C C 173.74 0.01 1 181 . 31 MET H H 8.67 0.01 1 182 . 31 MET N N 124.25 0.24 1 183 . 31 MET HA H 5.02 0.01 1 184 . 31 MET CA C 54.73 0.01 1 185 . 31 MET CB C 35.19 0.01 1 186 . 31 MET C C 176.32 0.01 1 187 . 32 ASP H H 8.98 0.01 1 188 . 32 ASP N N 126.86 0.24 1 189 . 32 ASP HA H 4.69 0.01 1 190 . 32 ASP CA C 52.12 0.01 1 191 . 32 ASP CB C 41.65 0.01 1 192 . 32 ASP C C 178.28 0.01 1 193 . 33 LYS H H 8.26 0.01 1 194 . 33 LYS N N 116.90 0.24 1 195 . 33 LYS HA H 4.02 0.01 1 196 . 33 LYS CA C 57.92 0.01 1 197 . 33 LYS CB C 31.84 0.01 1 198 . 33 LYS C C 179.26 0.01 1 199 . 34 SER H H 8.35 0.01 1 200 . 34 SER N N 114.77 0.24 1 201 . 34 SER HA H 4.42 0.01 1 202 . 34 SER CA C 58.31 0.01 1 203 . 34 SER CB C 63.74 0.01 1 204 . 34 SER C C 174.37 0.01 1 205 . 35 GLY H H 7.98 0.01 1 206 . 35 GLY N N 109.08 0.24 1 207 . 35 GLY HA2 H 3.93 0.01 2 208 . 35 GLY CA C 44.84 0.01 1 209 . 35 GLY C C 173.96 0.01 1 210 . 36 ASN H H 8.12 0.01 5 211 . 36 ASN N N 118.80 0.24 5 212 . 36 ASN HA H 4.83 0.01 1 213 . 36 ASN CA C 51.79 0.01 1 214 . 36 ASN CB C 39.20 0.01 1 215 . 36 ASN C C 173.88 0.01 1 216 . 37 MET H H 9.28 0.01 1 217 . 37 MET N N 116.67 0.24 1 218 . 37 MET HA H 5.25 0.01 1 219 . 37 MET CA C 53.51 0.01 1 220 . 37 MET CB C 33.96 0.01 1 221 . 37 MET C C 175.63 0.01 1 222 . 38 THR H H 8.78 0.01 1 223 . 38 THR N N 116.43 0.24 1 224 . 38 THR HA H 4.98 0.01 1 225 . 38 THR CA C 60.37 0.01 1 226 . 38 THR CB C 71.49 0.01 1 227 . 38 THR C C 174.33 0.01 1 228 . 39 LEU H H 8.30 0.01 1 229 . 39 LEU N N 124.49 0.24 1 230 . 39 LEU HA H 5.45 0.01 1 231 . 39 LEU CA C 52.69 0.01 1 232 . 39 LEU CB C 45.82 0.01 1 233 . 39 LEU C C 176.02 0.01 1 234 . 40 SER H H 8.82 0.01 1 235 . 40 SER N N 117.85 0.24 1 236 . 40 SER HA H 5.23 0.01 1 237 . 40 SER CA C 57.51 0.01 1 238 . 40 SER CB C 65.52 0.01 1 239 . 40 SER C C 172.03 0.01 1 240 . 41 VAL H H 8.70 0.01 1 241 . 41 VAL N N 114.06 0.24 1 242 . 41 VAL HA H 4.83 0.01 1 243 . 41 VAL CA C 58.28 0.01 1 244 . 41 VAL CB C 36.17 0.01 1 245 . 41 VAL C C 174.81 0.01 1 246 . 42 GLU H H 9.21 0.01 1 247 . 42 GLU N N 122.12 0.24 1 248 . 42 GLU HA H 4.31 0.01 1 249 . 42 GLU CA C 56.69 0.01 1 250 . 42 GLU CB C 29.06 0.01 1 251 . 42 GLU C C 179.19 0.01 1 252 . 43 LYS H H 8.99 0.01 1 253 . 43 LYS N N 124.02 0.24 1 254 . 43 LYS HA H 3.67 0.01 1 255 . 43 LYS CA C 60.29 0.01 1 256 . 43 LYS CB C 32.17 0.01 1 257 . 43 LYS C C 179.16 0.01 1 258 . 44 GLU H H 9.23 0.01 1 259 . 44 GLU N N 116.67 0.24 1 260 . 44 GLU HA H 4.07 0.01 1 261 . 44 GLU CA C 58.74 0.01 1 262 . 44 GLU CB C 28.73 0.01 1 263 . 44 GLU C C 176.96 0.01 1 264 . 45 ASP H H 7.92 0.01 1 265 . 45 ASP N N 117.14 0.24 1 266 . 45 ASP HA H 4.96 0.01 1 267 . 45 ASP CA C 54.16 0.01 1 268 . 45 ASP CB C 43.04 0.01 1 269 . 45 ASP C C 175.77 0.01 1 270 . 46 PHE H H 7.60 0.01 1 271 . 46 PHE N N 122.12 0.24 1 272 . 46 PHE HA H 3.65 0.01 1 273 . 46 PHE CA C 63.15 0.01 1 274 . 46 PHE CB C 40.18 0.01 1 275 . 46 PHE C C 175.46 0.01 1 276 . 47 VAL H H 8.37 0.01 1 277 . 47 VAL N N 117.38 0.24 1 278 . 47 VAL HA H 3.38 0.01 1 279 . 47 VAL CA C 66.59 0.01 1 280 . 47 VAL CB C 30.86 0.01 1 281 . 47 VAL C C 179.56 0.01 1 282 . 48 ARG H H 8.53 0.01 1 283 . 48 ARG N N 122.83 0.24 1 284 . 48 ARG HA H 3.92 0.01 1 285 . 48 ARG CA C 59.39 0.01 1 286 . 48 ARG CB C 30.20 0.01 1 287 . 48 ARG C C 177.97 0.01 1 288 . 49 ALA H H 8.50 0.01 5 289 . 49 ALA N N 119.75 0.24 5 290 . 49 ALA HA H 3.76 0.01 1 291 . 49 ALA CA C 54.73 0.01 1 292 . 49 ALA CB C 19.41 0.01 1 293 . 49 ALA C C 178.92 0.01 1 294 . 50 ILE H H 8.12 0.01 1 295 . 50 ILE N N 117.14 0.24 1 296 . 50 ILE HA H 3.57 0.01 1 297 . 50 ILE CA C 62.91 0.01 1 298 . 50 ILE CB C 36.50 0.01 1 299 . 50 ILE C C 177.86 0.01 1 300 . 51 THR H H 7.92 0.01 1 301 . 51 THR N N 117.38 0.24 1 302 . 51 THR HA H 4.19 0.01 1 303 . 51 THR CA C 66.42 0.01 1 304 . 51 THR CB C 68.55 0.01 1 305 . 51 THR C C 176.95 0.01 1 306 . 52 ILE H H 7.98 0.01 1 307 . 52 ILE N N 121.41 0.24 1 308 . 52 ILE HA H 3.59 0.01 1 309 . 52 ILE CA C 64.95 0.01 1 310 . 52 ILE CB C 38.46 0.01 1 311 . 52 ILE C C 179.48 0.01 1 312 . 53 LEU H H 8.23 0.01 1 313 . 53 LEU N N 119.51 0.24 1 314 . 53 LEU HA H 3.89 0.01 1 315 . 53 LEU CA C 58.82 0.01 1 316 . 53 LEU CB C 40.18 0.01 1 317 . 53 LEU C C 179.54 0.01 1 318 . 54 ASN H H 9.14 0.01 1 319 . 54 ASN N N 119.75 0.24 1 320 . 54 ASN HA H 4.60 0.01 1 321 . 54 ASN CA C 55.71 0.01 1 322 . 54 ASN CB C 37.64 0.01 1 323 . 54 ASN C C 179.34 0.01 1 324 . 55 ASN H H 8.50 0.01 5 325 . 55 ASN N N 118.33 0.24 5 326 . 55 ASN HA H 4.42 0.01 1 327 . 55 ASN CA C 54.65 0.01 1 328 . 55 ASN CB C 37.64 0.01 1 329 . 55 ASN C C 175.92 0.01 1 330 . 56 ASN H H 7.54 0.01 1 331 . 56 ASN N N 115.95 0.24 1 332 . 56 ASN HA H 4.67 0.01 1 333 . 56 ASN CA C 53.10 0.01 1 334 . 56 ASN CB C 41.65 0.01 1 335 . 56 ASN C C 173.36 0.01 1 336 . 57 GLY H H 7.51 0.01 1 337 . 57 GLY N N 106.23 0.24 1 338 . 57 GLY HA2 H 3.44 0.01 1 339 . 57 GLY HA3 H 3.44 0.01 1 340 . 57 GLY CA C 46.23 0.01 1 341 . 57 GLY C C 173.12 0.01 1 342 . 58 PHE H H 8.00 0.01 1 343 . 58 PHE N N 115.95 0.24 1 344 . 58 PHE CA C 55.14 0.01 1 345 . 58 PHE CB C 41.98 0.01 1 346 . 58 PHE C C 173.91 0.01 1 347 . 63 PHE HA H 4.42 0.01 1 348 . 63 PHE CA C 57.76 0.01 1 349 . 63 PHE CB C 39.65 0.01 1 350 . 63 PHE C C 175.33 0.01 1 351 . 64 ALA H H 7.92 0.01 1 352 . 64 ALA N N 123.78 0.24 1 353 . 64 ALA HA H 4.09 0.01 1 354 . 64 ALA CA C 52.61 0.01 1 355 . 64 ALA CB C 19.16 0.01 1 356 . 64 ALA C C 177.25 0.01 1 357 . 65 ASP H H 8.17 0.01 1 358 . 65 ASP N N 118.80 0.24 1 359 . 65 ASP HA H 4.50 0.01 1 360 . 65 ASP CA C 54.08 0.01 1 361 . 65 ASP CB C 40.67 0.01 1 362 . 65 ASP C C 176.27 0.01 1 363 . 66 ILE H H 7.83 0.01 1 364 . 66 ILE N N 119.75 0.24 1 365 . 66 ILE HA H 4.27 0.01 1 366 . 66 ILE CA C 60.86 0.01 1 367 . 66 ILE CB C 38.62 0.01 1 368 . 66 ILE C C 176.00 0.01 1 369 . 67 GLU H H 8.28 0.01 1 370 . 67 GLU N N 124.02 0.24 1 371 . 67 GLU HA H 4.17 0.01 1 372 . 67 GLU CA C 56.20 0.01 1 373 . 67 GLU CB C 29.88 0.01 1 374 . 67 GLU C C 176.08 0.01 1 375 . 68 VAL H H 8.09 0.01 1 376 . 68 VAL N N 122.02 0.24 1 377 . 68 VAL HA H 4.27 0.01 1 378 . 68 VAL CA C 62.01 0.01 1 379 . 68 VAL CB C 32.33 0.01 1 380 . 68 VAL C C 175.65 0.01 1 381 . 69 ILE H H 8.03 0.01 1 382 . 69 ILE N N 125.20 0.24 1 383 . 69 ILE HA H 4.04 0.01 1 384 . 69 ILE CA C 60.37 0.01 1 385 . 69 ILE CB C 38.46 0.01 1 386 . 69 ILE C C 174.53 0.01 1 387 . 70 PHE H H 8.22 0.01 1 388 . 70 PHE N N 124.73 0.24 1 389 . 70 PHE CA C 54.98 0.01 1 390 . 70 PHE CB C 38.71 0.01 1 391 . 70 PHE C C 173.51 0.01 1 392 . 73 SER HA H 4.25 0.01 1 393 . 73 SER CA C 58.30 0.01 1 394 . 73 SER CB C 62.96 0.01 1 395 . 73 SER C C 174.80 0.01 1 396 . 74 GLN H H 8.27 0.01 1 397 . 74 GLN N N 121.41 0.24 1 398 . 74 GLN HA H 4.19 0.01 1 399 . 74 GLN CA C 55.71 0.01 1 400 . 74 GLN CB C 29.22 0.01 1 401 . 74 GLN C C 175.72 0.01 1 402 . 75 LEU H H 8.05 0.01 1 403 . 75 LEU N N 122.59 0.24 1 404 . 75 LEU HA H 4.21 0.01 1 405 . 75 LEU CA C 55.14 0.01 1 406 . 75 LEU CB C 41.98 0.01 1 407 . 75 LEU C C 177.07 0.01 1 408 . 76 VAL H H 7.89 0.01 1 409 . 76 VAL N N 120.46 0.24 1 410 . 76 VAL HA H 3.98 0.01 1 411 . 76 VAL CA C 61.44 0.01 1 412 . 76 VAL CB C 32.41 0.01 1 413 . 76 VAL C C 175.53 0.01 1 414 . 77 ALA H H 8.27 0.01 1 415 . 77 ALA N N 127.81 0.24 1 416 . 77 ALA HA H 4.20 0.01 1 417 . 77 ALA CA C 51.79 0.01 1 418 . 77 ALA CB C 19.08 0.01 1 419 . 77 ALA C C 177.27 0.01 1 420 . 78 SER H H 8.22 0.01 1 421 . 78 SER N N 116.43 0.24 1 422 . 78 SER CA C 55.71 0.01 1 423 . 78 SER CB C 62.91 0.01 1 424 . 78 SER C C 177.27 0.01 1 425 . 82 GLU HA H 4.09 0.01 1 426 . 82 GLU CA C 57.69 0.01 1 427 . 82 GLU CB C 29.33 0.01 1 428 . 82 GLU C C 177.26 0.01 1 429 . 83 ASN H H 8.28 0.01 1 430 . 83 ASN N N 118.56 0.24 1 431 . 83 ASN HA H 4.17 0.01 1 432 . 83 ASN CA C 54.16 0.01 1 433 . 83 ASN CB C 38.13 0.01 1 434 . 83 ASN C C 175.97 0.01 1 435 . 84 ALA H H 8.06 0.01 1 436 . 84 ALA N N 123.07 0.24 1 437 . 84 ALA HA H 4.13 0.01 1 438 . 84 ALA CA C 53.59 0.01 1 439 . 84 ALA CB C 18.43 0.01 1 440 . 84 ALA C C 178.99 0.01 1 441 . 85 LYS H H 8.01 0.01 1 442 . 85 LYS N N 119.51 0.24 1 443 . 85 LYS HA H 4.15 0.01 1 444 . 85 LYS CA C 57.27 0.01 1 445 . 85 LYS CB C 32.08 0.01 1 446 . 85 LYS C C 177.48 0.01 1 447 . 86 ILE H H 7.79 0.01 1 448 . 86 ILE N N 119.51 0.24 1 449 . 86 ILE HA H 3.86 0.01 1 450 . 86 ILE CA C 62.74 0.01 1 451 . 86 ILE CB C 38.05 0.01 1 452 . 86 ILE C C 177.53 0.01 1 453 . 87 ASN H H 8.25 0.01 1 454 . 87 ASN N N 120.22 0.24 1 455 . 87 ASN HA H 4.50 0.01 1 456 . 87 ASN CA C 54.98 0.01 1 457 . 87 ASN CB C 38.38 0.01 1 458 . 87 ASN C C 176.03 0.01 1 459 . 88 TYR H H 7.87 0.01 1 460 . 88 TYR N N 119.99 0.24 1 461 . 88 TYR CA C 59.56 0.01 1 462 . 88 TYR CB C 40.67 0.01 1 463 . 89 LEU H H 7.64 0.01 5 464 . 89 LEU N N 119.51 0.24 5 465 . 90 LYS HA H 4.09 0.01 1 466 . 90 LYS CA C 57.76 0.01 1 467 . 90 LYS CB C 31.62 0.01 1 468 . 90 LYS C C 178.82 0.01 1 469 . 91 GLU H H 8.49 0.01 1 470 . 91 GLU N N 119.27 0.24 1 471 . 91 GLU HA H 3.46 0.01 1 472 . 91 GLU CA C 60.44 0.01 1 473 . 91 GLU CB C 28.79 0.01 1 474 . 91 GLU C C 178.82 0.01 1 475 . 92 GLN H H 8.00 0.01 1 476 . 92 GLN N N 115.78 0.24 1 477 . 92 GLN HA H 3.85 0.01 1 478 . 92 GLN CA C 58.30 0.01 1 479 . 92 GLN CB C 28.79 0.01 1 480 . 93 ASP H H 7.86 0.01 1 481 . 93 ASP N N 120.52 0.24 1 482 . 93 ASP HA H 4.33 0.01 1 483 . 93 ASP CA C 57.23 0.01 1 484 . 93 ASP CB C 40.56 0.01 1 485 . 93 ASP C C 179.03 0.01 1 486 . 94 ILE H H 8.03 0.01 1 487 . 94 ILE N N 119.99 0.24 1 488 . 94 ILE HA H 3.53 0.01 1 489 . 94 ILE CA C 64.81 0.01 1 490 . 94 ILE CB C 37.53 0.01 1 491 . 94 ILE C C 178.07 0.01 1 492 . 95 GLU H H 8.50 0.01 1 493 . 95 GLU N N 119.99 0.24 1 494 . 95 GLU HA H 3.69 0.01 1 495 . 95 GLU CA C 59.65 0.01 1 496 . 95 GLU CB C 28.76 0.01 1 497 . 95 GLU C C 179.35 0.01 1 498 . 96 ARG H H 7.94 0.01 1 499 . 96 ARG N N 118.80 0.24 1 500 . 96 ARG HA H 3.84 0.01 1 501 . 96 ARG CA C 59.30 0.01 1 502 . 96 ARG CB C 29.70 0.01 1 503 . 96 ARG C C 179.44 0.01 1 504 . 97 LEU H H 7.49 0.01 1 505 . 97 LEU N N 119.99 0.24 1 506 . 97 LEU HA H 3.92 0.01 1 507 . 97 LEU CA C 57.58 0.01 1 508 . 97 LEU CB C 42.18 0.01 1 509 . 97 LEU C C 180.23 0.01 1 510 . 98 LEU H H 8.50 0.01 5 511 . 98 LEU N N 119.75 0.24 5 512 . 98 LEU HA H 3.82 0.01 1 513 . 98 LEU CA C 57.24 0.01 1 514 . 98 LEU CB C 42.01 0.01 1 515 . 98 LEU C C 178.48 0.01 1 516 . 99 SER H H 7.79 0.01 1 517 . 99 SER N N 110.50 0.24 1 518 . 99 SER HA H 3.86 0.01 1 519 . 99 SER CA C 60.34 0.01 1 520 . 99 SER CB C 62.89 0.01 1 521 . 99 SER C C 174.21 0.01 1 522 . 100 LYS H H 7.03 0.01 1 523 . 100 LYS N N 117.61 0.24 1 524 . 100 LYS HA H 4.15 0.01 1 525 . 100 LYS CA C 55.25 0.01 1 526 . 100 LYS CB C 32.15 0.01 1 527 . 100 LYS C C 177.45 0.01 1 528 . 101 ILE H H 7.59 0.01 1 529 . 101 ILE N N 125.20 0.24 1 530 . 101 ILE CA C 59.50 0.01 1 531 . 101 ILE CB C 37.41 0.01 1 532 . 101 ILE C C 174.60 0.01 1 533 . 102 PRO HA H 4.13 0.01 1 534 . 102 PRO CA C 63.86 0.01 1 535 . 102 PRO CB C 31.17 0.01 1 536 . 102 PRO C C 176.62 0.01 1 537 . 103 GLY H H 8.44 0.01 1 538 . 103 GLY N N 110.26 0.24 1 539 . 103 GLY HA2 H 3.44 0.01 1 540 . 103 GLY HA3 H 4.25 0.01 1 541 . 103 GLY CA C 44.67 0.01 1 542 . 103 GLY C C 173.88 0.01 1 543 . 104 VAL H H 7.65 0.01 1 544 . 104 VAL N N 119.99 0.24 1 545 . 104 VAL HA H 3.72 0.01 1 546 . 104 VAL CA C 63.52 0.01 1 547 . 104 VAL CB C 31.17 0.01 1 548 . 104 VAL C C 176.30 0.01 1 549 . 105 ILE H H 8.98 0.01 1 550 . 105 ILE N N 127.34 0.24 1 551 . 105 ILE HA H 4.13 0.01 1 552 . 105 ILE CA C 61.45 0.01 1 553 . 105 ILE CB C 38.31 0.01 1 554 . 105 ILE C C 175.62 0.01 1 555 . 106 ASP H H 7.83 0.01 1 556 . 106 ASP N N 117.38 0.24 1 557 . 106 ASP HA H 4.77 0.01 1 558 . 106 ASP CA C 52.59 0.01 1 559 . 106 ASP CB C 43.56 0.01 1 560 . 106 ASP C C 173.80 0.01 1 561 . 107 CYS H H 8.66 0.01 1 562 . 107 CYS N N 115.72 0.24 1 563 . 107 CYS HA H 5.26 0.01 1 564 . 107 CYS CA C 56.12 0.01 1 565 . 107 CYS CB C 29.87 0.01 1 566 . 107 CYS C C 172.08 0.01 1 567 . 108 SER H H 8.89 0.01 1 568 . 108 SER N N 115.01 0.24 1 569 . 108 SER HA H 4.85 0.01 1 570 . 108 SER CA C 56.29 0.01 1 571 . 108 SER CB C 65.41 0.01 1 572 . 108 SER C C 173.33 0.01 1 573 . 109 VAL H H 9.92 0.01 1 574 . 109 VAL N N 127.57 0.24 1 575 . 109 VAL HA H 4.50 0.01 1 576 . 109 VAL CA C 60.85 0.01 1 577 . 109 VAL CB C 34.00 0.01 1 578 . 109 VAL C C 173.75 0.01 1 579 . 110 SER H H 8.66 0.01 1 580 . 110 SER N N 120.22 0.24 1 581 . 110 SER HA H 4.91 0.01 1 582 . 110 SER CA C 55.52 0.01 1 583 . 110 SER CB C 64.46 0.01 1 584 . 110 SER C C 174.26 0.01 1 585 . 111 LEU H H 10.14 0.01 1 586 . 111 LEU N N 128.28 0.24 1 587 . 111 LEU HA H 4.66 0.01 1 588 . 111 LEU CA C 53.45 0.01 1 589 . 111 LEU CB C 43.38 0.01 1 590 . 111 LEU C C 175.56 0.01 1 591 . 112 ASN H H 8.54 0.01 1 592 . 112 ASN N N 122.36 0.24 1 593 . 112 ASN HA H 4.81 0.01 1 594 . 112 ASN CA C 52.59 0.01 1 595 . 112 ASN CB C 38.65 0.01 1 596 . 112 ASN C C 174.01 0.01 1 597 . 113 VAL H H 8.20 0.01 1 598 . 113 VAL N N 120.70 0.24 1 599 . 113 VAL HA H 4.20 0.01 1 600 . 113 VAL CA C 60.68 0.01 1 601 . 113 VAL CB C 32.80 0.01 1 602 . 113 VAL C C 175.60 0.01 1 603 . 114 ASN H H 8.62 0.01 5 604 . 114 ASN N N 123.54 0.24 5 605 . 114 ASN HA H 4.60 0.01 1 606 . 114 ASN CA C 52.68 0.01 1 607 . 114 ASN CB C 39.25 0.01 1 608 . 114 ASN C C 179.32 0.01 1 609 . 115 ASN H H 8.50 0.01 5 610 . 115 ASN N N 118.33 0.24 5 611 . 115 ASN HA H 4.50 0.01 1 612 . 115 ASN CA C 53.62 0.01 1 613 . 115 ASN CB C 38.48 0.01 1 614 . 115 ASN C C 175.46 0.01 1 615 . 116 ASN H H 8.39 0.01 1 616 . 116 ASN N N 117.14 0.24 1 617 . 116 ASN HA H 4.52 0.01 1 618 . 116 ASN CA C 53.36 0.01 1 619 . 116 ASN CB C 38.57 0.01 1 620 . 116 ASN C C 175.13 0.01 1 621 . 117 GLU H H 8.31 0.01 1 622 . 117 GLU N N 119.51 0.24 1 623 . 117 GLU HA H 4.19 0.01 1 624 . 117 GLU CA C 56.72 0.01 1 625 . 117 GLU CB C 29.79 0.01 1 626 . 117 GLU C C 176.38 0.01 1 627 . 118 SER H H 8.30 0.01 1 628 . 118 SER N N 113.11 0.24 1 629 . 118 SER HA H 4.27 0.01 1 630 . 118 SER CA C 58.79 0.01 1 631 . 118 SER CB C 63.35 0.01 1 632 . 118 SER C C 174.03 0.01 1 633 . 119 GLN H H 7.66 0.01 1 634 . 119 GLN N N 120.70 0.24 1 635 . 119 GLN CA C 52.59 0.01 1 636 . 119 GLN CB C 29.27 0.01 1 637 . 119 GLN C C 173.01 0.01 1 638 . 120 PRO CA C 62.92 0.01 1 639 . 120 PRO CB C 31.60 0.01 1 640 . 120 PRO C C 177.35 0.01 1 641 . 121 SER H H 8.22 0.01 1 642 . 121 SER N N 114.53 0.24 1 643 . 121 SER HA H 4.59 0.01 1 644 . 121 SER CA C 58.27 0.01 1 645 . 121 SER CB C 63.86 0.01 1 646 . 121 SER C C 173.71 0.01 1 647 . 122 SER H H 8.45 0.01 1 648 . 122 SER N N 114.77 0.24 1 649 . 122 SER HA H 4.69 0.01 1 650 . 122 SER CA C 57.32 0.01 1 651 . 122 SER CB C 65.93 0.01 1 652 . 122 SER C C 171.98 0.01 1 653 . 123 ALA H H 8.42 0.01 5 654 . 123 ALA N N 118.80 0.24 5 655 . 123 ALA HA H 5.22 0.01 1 656 . 123 ALA CA C 50.53 0.01 1 657 . 123 ALA CB C 24.02 0.01 1 658 . 123 ALA C C 174.96 0.01 1 659 . 124 ALA H H 9.00 0.01 1 660 . 124 ALA N N 125.68 0.24 1 661 . 124 ALA HA H 5.10 0.01 1 662 . 124 ALA CA C 50.87 0.01 1 663 . 124 ALA CB C 20.58 0.01 1 664 . 124 ALA C C 175.96 0.01 1 665 . 125 VAL H H 8.95 0.01 1 666 . 125 VAL N N 124.02 0.24 1 667 . 125 VAL HA H 4.65 0.01 1 668 . 125 VAL CA C 60.42 0.01 1 669 . 125 VAL CB C 34.44 0.01 1 670 . 125 VAL C C 173.83 0.01 1 671 . 126 LEU H H 9.05 0.01 1 672 . 126 LEU N N 132.32 0.24 1 673 . 126 LEU HA H 5.14 0.01 1 674 . 126 LEU CA C 53.19 0.01 1 675 . 126 LEU CB C 43.81 0.01 1 676 . 126 LEU C C 175.20 0.01 1 677 . 127 VAL H H 9.07 0.01 1 678 . 127 VAL N N 125.20 0.24 1 679 . 127 VAL HA H 4.25 0.01 1 680 . 127 VAL CA C 60.68 0.01 1 681 . 127 VAL CB C 34.95 0.01 1 682 . 127 VAL C C 172.98 0.01 1 683 . 128 ILE H H 8.47 0.01 1 684 . 128 ILE N N 126.39 0.24 1 685 . 128 ILE HA H 4.95 0.01 1 686 . 128 ILE CA C 58.10 0.01 1 687 . 128 ILE CB C 36.50 0.01 1 688 . 128 ILE C C 175.72 0.01 1 689 . 129 SER H H 8.92 0.01 1 690 . 129 SER N N 122.12 0.24 1 691 . 129 SER HA H 5.16 0.01 1 692 . 129 SER CA C 55.77 0.01 1 693 . 129 SER CB C 66.70 0.01 1 694 . 129 SER C C 174.15 0.01 1 695 . 130 SER H H 8.72 0.01 1 696 . 130 SER N N 117.61 0.24 1 697 . 130 SER CA C 55.86 0.01 1 698 . 130 SER CB C 63.43 0.01 1 699 . 139 VAL HA H 3.33 0.01 1 700 . 139 VAL CA C 67.57 0.01 1 701 . 139 VAL CB C 31.27 0.01 1 702 . 139 VAL C C 177.37 0.01 1 703 . 140 ILE H H 8.08 0.01 1 704 . 140 ILE N N 118.80 0.24 1 705 . 140 ILE HA H 3.68 0.01 1 706 . 140 ILE CA C 63.17 0.01 1 707 . 140 ILE CB C 37.02 0.01 1 708 . 140 ILE C C 177.40 0.01 1 709 . 141 GLN H H 7.50 0.01 1 710 . 141 GLN N N 121.65 0.24 1 711 . 141 GLN HA H 4.01 0.01 1 712 . 141 GLN CA C 58.79 0.01 1 713 . 141 GLN CB C 27.98 0.01 1 714 . 141 GLN C C 179.16 0.01 1 715 . 142 ILE H H 7.99 0.01 1 716 . 142 ILE N N 119.75 0.24 1 717 . 142 ILE HA H 3.37 0.01 1 718 . 142 ILE CA C 64.93 0.01 1 719 . 142 ILE CB C 36.90 0.01 1 720 . 142 ILE C C 177.35 0.01 1 721 . 143 LYS H H 8.58 0.01 1 722 . 143 LYS N N 117.38 0.24 1 723 . 143 LYS HA H 3.52 0.01 1 724 . 143 LYS CA C 61.36 0.01 1 725 . 143 LYS CB C 33.00 0.01 1 726 . 143 LYS C C 178.14 0.01 1 727 . 144 ASN H H 8.17 0.01 1 728 . 144 ASN N N 115.95 0.24 1 729 . 144 ASN HA H 4.26 0.01 1 730 . 144 ASN CA C 55.76 0.01 1 731 . 144 ASN CB C 38.09 0.01 1 732 . 144 ASN C C 177.23 0.01 1 733 . 145 LEU H H 7.78 0.01 1 734 . 145 LEU N N 121.71 0.24 1 735 . 145 LEU HA H 3.97 0.01 1 736 . 145 LEU CA C 57.63 0.01 1 737 . 145 LEU CB C 42.17 0.01 1 738 . 145 LEU C C 179.67 0.01 1 739 . 146 VAL H H 7.76 0.01 5 740 . 146 VAL N N 119.04 0.24 5 741 . 146 VAL HA H 3.21 0.01 1 742 . 146 VAL CA C 66.62 0.01 1 743 . 146 VAL CB C 30.82 0.01 1 744 . 146 VAL C C 177.40 0.01 1 745 . 147 LYS H H 8.41 0.01 1 746 . 147 LYS N N 119.75 0.24 1 747 . 147 LYS HA H 3.64 0.01 1 748 . 147 LYS CA C 59.39 0.01 1 749 . 147 LYS CB C 31.85 0.01 1 750 . 147 LYS C C 177.64 0.01 1 751 . 148 ASN H H 7.92 0.01 1 752 . 148 ASN N N 113.35 0.24 1 753 . 148 ASN HA H 4.40 0.01 1 754 . 148 ASN CA C 54.57 0.01 1 755 . 148 ASN CB C 38.13 0.01 1 756 . 148 ASN C C 176.41 0.01 1 757 . 149 SER H H 7.54 0.01 1 758 . 149 SER N N 113.35 0.24 1 759 . 149 SER HA H 4.34 0.01 1 760 . 149 SER CA C 60.08 0.01 1 761 . 149 SER CB C 64.46 0.01 1 762 . 149 SER C C 173.10 0.01 1 763 . 150 VAL H H 7.34 0.01 1 764 . 150 VAL N N 120.46 0.24 1 765 . 150 VAL HA H 4.19 0.01 1 766 . 150 VAL CA C 60.42 0.01 1 767 . 150 VAL CB C 32.97 0.01 1 768 . 150 VAL C C 174.30 0.01 1 769 . 151 ASP H H 8.23 0.01 1 770 . 151 ASP N N 124.02 0.24 1 771 . 151 ASP HA H 4.36 0.01 1 772 . 151 ASP CA C 56.12 0.01 1 773 . 151 ASP CB C 40.89 0.01 1 774 . 151 ASP C C 176.64 0.01 1 775 . 152 ASP H H 8.34 0.01 1 776 . 152 ASP N N 115.95 0.24 1 777 . 152 ASP HA H 4.22 0.01 1 778 . 152 ASP CA C 55.17 0.01 1 779 . 152 ASP CB C 40.20 0.01 1 780 . 152 ASP C C 175.16 0.01 1 781 . 153 LEU H H 7.60 0.01 1 782 . 153 LEU N N 120.70 0.24 1 783 . 153 LEU HA H 4.24 0.01 1 784 . 153 LEU CA C 54.14 0.01 1 785 . 153 LEU CB C 43.21 0.01 1 786 . 153 LEU C C 175.82 0.01 1 787 . 154 LYS H H 8.37 0.01 1 788 . 154 LYS N N 123.54 0.24 1 789 . 154 LYS HA H 4.34 0.01 1 790 . 154 LYS CA C 54.66 0.01 1 791 . 154 LYS CB C 32.80 0.01 1 792 . 154 LYS C C 178.23 0.01 1 793 . 155 LEU H H 8.67 0.01 5 794 . 155 LEU N N 122.59 0.24 5 795 . 155 LEU HA H 3.66 0.01 1 796 . 155 LEU CA C 58.18 0.01 1 797 . 155 LEU CB C 42.18 0.01 1 798 . 155 LEU C C 179.39 0.01 1 799 . 156 GLU H H 9.38 0.01 1 800 . 156 GLU N N 115.07 0.24 1 801 . 156 GLU HA H 4.03 0.01 1 802 . 156 GLU CA C 57.93 0.01 1 803 . 156 GLU CB C 28.24 0.01 1 804 . 156 GLU C C 176.51 0.01 1 805 . 157 ASN H H 7.71 0.01 1 806 . 157 ASN N N 117.14 0.24 1 807 . 157 ASN HA H 4.97 0.01 1 808 . 157 ASN CA C 52.50 0.01 1 809 . 157 ASN CB C 39.17 0.01 1 810 . 157 ASN C C 173.32 0.01 1 811 . 158 ILE H H 7.29 0.01 1 812 . 158 ILE N N 120.22 0.24 1 813 . 158 ILE HA H 4.60 0.01 1 814 . 158 ILE CA C 60.25 0.01 1 815 . 158 ILE CB C 39.17 0.01 1 816 . 158 ILE C C 174.67 0.01 1 817 . 159 SER H H 8.67 0.01 5 818 . 159 SER N N 122.59 0.24 5 819 . 159 SER HA H 4.69 0.01 1 820 . 159 SER CA C 56.12 0.01 1 821 . 159 SER CB C 64.03 0.01 1 822 . 159 SER C C 173.54 0.01 1 823 . 160 VAL H H 8.56 0.01 1 824 . 160 VAL N N 124.73 0.24 1 825 . 160 VAL HA H 4.75 0.01 1 826 . 160 VAL CA C 60.59 0.01 1 827 . 160 VAL CB C 33.92 0.01 1 828 . 160 VAL C C 174.45 0.01 1 829 . 161 VAL H H 8.72 0.01 1 830 . 161 VAL N N 129.71 0.24 1 831 . 161 VAL HA H 4.09 0.01 1 832 . 161 VAL CA C 61.19 0.01 1 833 . 161 VAL CB C 34.35 0.01 1 834 . 161 VAL C C 173.71 0.01 1 835 . 162 ILE H H 8.42 0.01 1 836 . 162 ILE N N 126.39 0.24 1 837 . 162 ILE HA H 4.87 0.01 1 838 . 162 ILE CA C 59.30 0.01 1 839 . 162 ILE CB C 38.65 0.01 1 840 . 162 ILE C C 175.92 0.01 1 841 . 163 LYS H H 9.06 0.01 1 842 . 163 LYS N N 128.05 0.24 1 843 . 163 LYS HA H 4.63 0.01 1 844 . 163 LYS CA C 53.97 0.01 1 845 . 163 LYS CB C 35.30 0.01 1 846 . 163 LYS C C 174.79 0.01 1 847 . 164 SER H H 8.54 0.01 1 848 . 164 SER N N 116.67 0.24 1 849 . 164 SER HA H 4.83 0.01 1 850 . 164 SER CA C 57.15 0.01 1 851 . 164 SER CB C 64.12 0.01 1 852 . 164 SER C C 175.62 0.01 1 853 . 165 SER H H 8.42 0.01 1 854 . 165 SER N N 117.85 0.24 1 855 . 165 SER CA C 58.10 0.01 1 856 . 165 SER CB C 63.60 0.01 1 857 . 166 SER HA H 4.38 0.01 1 858 . 166 SER CA C 58.22 0.01 1 859 . 166 SER CB C 63.50 0.01 1 860 . 166 SER C C 175.09 0.01 1 861 . 167 GLY H H 8.28 0.01 1 862 . 167 GLY N N 110.26 0.24 1 863 . 167 GLY HA2 H 3.89 0.01 1 864 . 167 GLY HA3 H 3.89 0.01 1 865 . 167 GLY CA C 45.02 0.01 1 866 . 167 GLY C C 174.17 0.01 1 867 . 168 GLN H H 8.19 0.01 1 868 . 168 GLN N N 119.51 0.24 1 869 . 168 GLN HA H 4.28 0.01 1 870 . 168 GLN CA C 55.52 0.01 1 871 . 168 GLN CB C 29.19 0.01 1 872 . 168 GLN C C 175.62 0.01 1 873 . 169 ASP H H 8.34 0.01 1 874 . 169 ASP N N 121.41 0.24 1 875 . 169 ASP HA H 4.54 0.01 1 876 . 169 ASP CA C 53.97 0.01 1 877 . 169 ASP CB C 41.15 0.01 1 878 . 169 ASP C C 175.53 0.01 1 879 . 170 GLY H H 7.82 0.01 1 880 . 170 GLY N N 115.24 0.24 1 881 . 170 GLY CA C 45.91 0.01 1 882 . 170 GLY C C 179.02 0.01 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 603 13 '604,14' '653,43' '654,44' '463,67' '464,68' '210,91' '211,92' '163,121' '164,122' '739,145' '740,146' '510,288' '511,289' '609,324' '610,325' '817,793' '818,794' stop_ save_